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</style><div role="note" class="hatnote navigation-not-searchable">"RAF1" redirects here. For the aircraft engine, see <a href="RAF_1" title="RAF 1">RAF 1</a>.</div>

<table class="infobox" style="width:26.4em"><tbody><tr><th colspan="4" style="text-align:center;font-size:125%;font-weight:bold">RAF1</th></tr><tr><td colspan="4" style="text-align:center"><span typeof="mw:File"></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit">Available structures</th></tr><tr><th rowspan="2" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit;width:43px"><a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a></th><td colspan="2" style="background-color:light-dark(#eee, #27292d) !important;color:inherit">Ortholog search: <span class=""><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/searchResults.html?display=both&term=Q99N57%20or%20P04049%20or%20H7C155">PDBe</a> <a rel="nofollow" class="external text" href="https://www.rcsb.org/search?q=rcsb_polymer_entity_container_identifiers.reference_sequence_identifiers.database_name:UniProt%20AND%20rcsb_polymer_entity_container_identifiers.reference_sequence_identifiers.database_accession:Q99N57,P04049,H7C155">RCSB</a> </span></td></tr><tr><td><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr style="text-align:center"><th colspan="2" style="background-color:light-dark(#ddd, #404244) !important;color:inherit">List of PDB id codes</th></tr><tr><td colspan="2" style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><p><span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1C1Y">1C1Y</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1FAQ">1FAQ</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1FAR">1FAR</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1GUA">1GUA</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1RFA">1RFA</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3CU8">3CU8</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3IQJ">3IQJ</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3IQU">3IQU</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3IQV">3IQV</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3KUC">3KUC</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3KUD">3KUD</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3NKX">3NKX</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3O8I">3O8I</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3OMV">3OMV</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/4FJ3">4FJ3</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/4G0N">4G0N</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/4G3X">4G3X</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/4IEA">4IEA</a>, <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/4IHL">4IHL</a></span></p></td></tr></tbody></table></td></tr></tbody></table></td></tr><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit">Identifiers</th></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><span class=""><a href="Gene_nomenclature" title="Gene nomenclature">Aliases</a></span></th><td colspan="3" style="background:light-dark(#eee, #27292d) !important;color:inherit"><span class=""><a rel="nofollow" class="external text" href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/9829">RAF1</a></span>, Raf-1 proto-oncogene, serine/threonine kinase, CMD1NN, CRAF, NS5, Raf-1, c-Raf</td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">External IDs</th><td colspan="3" style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class=""><a href="Mendelian_Inheritance_in_Man" class="mw-redirect" title="Mendelian Inheritance in Man">OMIM</a>: <a rel="nofollow" class="external text" href="https://omim.org/entry/164760">164760</a>; <a href="Mouse_Genome_Informatics" title="Mouse Genome Informatics">MGI</a>: <a rel="nofollow" class="external text" href="http://www.informatics.jax.org/marker/MGI:97847">97847</a>; <a href="HomoloGene" title="HomoloGene">HomoloGene</a>: <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=homologene&dopt=HomoloGene&list_uids=48145">48145</a>; <a href="GeneCards" title="GeneCards">GeneCards</a>: <a rel="nofollow" class="external text" href="https://www.genecards.org/cgi-bin/carddisp.pl?gene=RAF1">RAF1</a>; <a href="Orthologous_MAtrix" title="Orthologous MAtrix">OMA</a>:<a rel="nofollow" class="external text" href="https://omabrowser.org/oma/vps/ENSG00000132155">RAF1 - orthologs</a></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit">Gene location (<a href="Laboratory_mouse" title="Laboratory mouse">Mouse</a>)</th></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><span typeof="mw:File"></span></td></tr><tr><th scope="row" width="15%" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="Chromosome" title="Chromosome">Chr.</a></th><td colspan="3" width="85%" style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class="">Chromosome 6 (mouse)<sup id="cite_ref-refGRCm38Ensembl_1-0" class="reference"><a href="#cite_note-refGRCm38Ensembl-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><div align="center"><div style="position: relative; width: 300px;"><span typeof="mw:File"></span><div style="position: absolute; left: 221.72523959487px; top: 2px; padding: 0;"><span typeof="mw:File"></span></div><div style="position: absolute; left: 227.7px; top: 19px; padding: 0;"><span typeof="mw:File"></span></div></div></div></td></tr><tr><th scope="row" rowspan="2" width="15%" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="Locus_(genetics)" title="Locus (genetics)">Band</a></th><td rowspan="2" width="35%" style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class="">6 E3|6 53.62 cM</span></td><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">Start</th><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class="">115,595,028 <a href="Base_pair" title="Base pair">bp</a><sup id="cite_ref-refGRCm38Ensembl_1-1" class="reference"><a href="#cite_note-refGRCm38Ensembl-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></span></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">End</th><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class="">115,653,596 <a href="Base_pair" title="Base pair">bp</a><sup id="cite_ref-refGRCm38Ensembl_1-2" class="reference"><a href="#cite_note-refGRCm38Ensembl-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></span></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit"><a href="Gene_expression" title="Gene expression">RNA expression</a> pattern</th></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a rel="nofollow" class="external text" href="https://www.bgee.org/">Bgee</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th><b><a href="Human_genome" title="Human genome">Human</a></b></th><th><b><a href="Laboratory_mouse" title="Laboratory mouse">Mouse</a> (ortholog)</b></th></tr><tr><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:center"><tbody><tr><td colspan="1"></td></tr><tr><td colspan="1"><div class="" style="margin:-12px 0px -10px 0px"><ul style="line-height:15%;margin:9px">n/a</ul></div></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:center"><tbody><tr><td colspan="1"><span class="" style="margin:-3px"><a rel="nofollow" class="external text" href="https://www.bgee.org/gene/ENSMUSG00000000441">Top expressed in</a></span></td></tr><tr><td colspan="1"><div class="" style="margin:-12px 0px -10px 0px"><ul style="line-height:15%;margin:9px"><li style="line-height: 137%;">granulocyte</li><br><li style="line-height: 137%;">epithelium of stomach</li><br><li style="line-height: 137%;">zygote</li><br><li style="line-height: 137%;">medullary collecting duct</li><br><li style="line-height: 137%;">ventricular zone</li><br><li style="line-height: 137%;">secondary oocyte</li><br><li style="line-height: 137%;">ganglionic eminence</li><br><li style="line-height: 137%;">temporal muscle</li><br><li style="line-height: 137%;">triceps brachii muscle</li><br><li style="line-height: 137%;">muscle of thigh</li></ul></div></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a rel="nofollow" class="external text" href="http://biogps.org/">BioGPS</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><span typeof="mw:File"></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><span class=""><a rel="nofollow" class="external text" href="http://biogps.org/gene/5894/">More reference expression data</a></span></td></tr></tbody></table></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit"><a href="Gene_ontology" class="mw-redirect" title="Gene ontology">Gene ontology</a></th></tr><tr><td style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit;font-weight:bold">Molecular function</td><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><div class="">

<ul><li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0016740">transferase activity</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0004672">protein kinase activity</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0000166">nucleotide binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0046872">metal ion binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0004674">protein serine/threonine kinase activity</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0031267">small GTPase binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005515">protein binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0042802">identical protein binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005524">ATP binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0016301">kinase activity</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0004709">MAP kinase kinase kinase activity</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0019899">enzyme binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0031434">mitogen-activated protein kinase kinase binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0008179">adenylate cyclase binding</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0010856">adenylate cyclase activator activity</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0046982">protein heterodimerization activity</a></li></ul>

</div></td></tr><tr><td style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit;font-weight:bold">Cellular component</td><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><div class="">

<ul><li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005737">cytoplasm</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005829">cytosol</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005794">Golgi apparatus</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0031143">pseudopodium</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0016020">membrane</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005886">plasma membrane</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005741">mitochondrial outer membrane</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005739">mitochondrion</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005634">nucleus</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0016607">nuclear speck</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0005622">intracellular anatomical structure</a></li></ul>

</div></td></tr><tr><td style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit;font-weight:bold">Biological process</td><td style="background-color:light-dark(#eee, #27292d) !important;color:inherit"><div class="">

<ul><li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0035994">response to muscle stretch</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0042981">regulation of apoptotic process</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0030154">cell differentiation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0043154">negative regulation of cysteine-type endopeptidase activity involved in apoptotic process</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0001934">positive regulation of protein phosphorylation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0035556">intracellular signal transduction</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0001666">response to hypoxia</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0035019">somatic stem cell population maintenance</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0016310">phosphorylation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0048538">thymus development</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0001678">cellular glucose homeostasis</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0031333">negative regulation of protein-containing complex assembly</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0042060">wound healing</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0002223">stimulatory C-type lectin receptor signaling pathway</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0043066">negative regulation of apoptotic process</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0000165">MAPK cascade</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0033138">positive regulation of peptidyl-serine phosphorylation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:2000145">regulation of cell motility</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0030168">platelet activation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0006468">protein phosphorylation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0007507">heart development</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0030878">thyroid gland development</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0034220">ion transmembrane transport</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0060324">face development</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0071550">death-inducing signaling complex assembly</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:1902042">negative regulation of extrinsic apoptotic signaling pathway via death domain receptors</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0045104">intermediate filament cytoskeleton organization</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0045595">regulation of cell differentiation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0008283">cell population proliferation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0035023">regulation of Rho protein signal transduction</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0007165">signal transduction</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0008285">negative regulation of cell population proliferation</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0045944">positive regulation of transcription by RNA polymerase II</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0035773">insulin secretion involved in cellular response to glucose stimulus</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0006915">apoptotic process</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0048011">neurotrophin TRK receptor signaling pathway</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0007275">multicellular organism development</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0009968">negative regulation of signal transduction</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0070374">positive regulation of ERK1 and ERK2 cascade</a></li>

<li><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0007190">activation of adenylate cyclase activity</a></li></ul>

</div></td></tr><tr><td colspan="4" style="background-color:light-dark(#eee, #27292d) !important;color:inherit;text-align:center">Sources:<a rel="nofollow" class="external text" href="http://amigo.geneontology.org/">Amigo</a> / <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/QuickGO/">QuickGO</a></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table class="collapsible" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:light-dark(#ddd, #404244) !important;color:inherit"><a href="Orthologs" class="mw-redirect" title="Orthologs">Orthologs</a></th></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">Species</th><td><b>Human</b></td><td><b>Mouse</b></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="Entrez" title="Entrez">Entrez</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=retrieve&dopt=default&list_uids=5894&rn=1">5894</a></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=retrieve&dopt=default&list_uids=110157&rn=1">110157</a></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="Ensembl" class="mw-redirect" title="Ensembl">Ensembl</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="http://www.ensembl.org/Homo_sapiens/geneview?gene=ENSG00000132155;db=core">ENSG00000132155</a></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="http://www.ensembl.org/Mus_musculus/geneview?gene=ENSMUSG00000000441;db=core">ENSMUSG00000000441</a></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="UniProt" title="UniProt">UniProt</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprot/P04049">P04049</a></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"></th></tr><tr><td colspan="1"><p class=""><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprot/Q99N57">Q99N57</a></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">RefSeq (mRNA)</th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class=""></th></tr><tr><td colspan="1"><p><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NM_002880">NM_002880</a></span></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class=""></th></tr><tr><td colspan="1"><p><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NM_029780">NM_029780</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NM_001356333">NM_001356333</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NM_001356334">NM_001356334</a></span></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">RefSeq (protein)</th><td><table class="collapsible collapsed" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_002871">NP_002871</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001341618">NP_001341618</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001341619">NP_001341619</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001341620">NP_001341620</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001341621">NP_001341621</a><br></th></tr><tr><td colspan="1"><p><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001341622">NP_001341622</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001341624">NP_001341624</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001341623">NP_001341623</a></span></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class=""></th></tr><tr><td colspan="1"><p><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_084056">NP_084056</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001343262">NP_001343262</a><br><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_001343263">NP_001343263</a></span></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit">Location (UCSC)</th><td><span class="">n/a</span></td><td><span class=""><a rel="nofollow" class="external text" href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Mouse&db=mm0&position=chr6:115595028-115653596">Chr 6: 115.6 – 115.65 Mb</a></span></td></tr><tr><th scope="row" style="background-color:light-dark(#c3fdb8, #003500) !important;color:inherit"><a href="PubMed" title="PubMed">PubMed</a> search</th><td><span class=""><sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup></span></td><td><span class=""><sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup></span></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><a href="Wikidata" title="Wikidata">Wikidata</a></td></tr><tr><td colspan="4" style="text-align:center;background-color:light-dark(#eee, #27292d) !important;color:inherit"><table style="padding:0;border:none;margin:0;width:100%;text-align:center"><tbody><tr><td colspan="2" style="background-color:light-dark(#eee, #27292d) !important;color:inherit;text-align:center"><a href="https://www.wikidata.org/wiki/Q14903573" class="extiw external" title="d:Q14903573">View/Edit Human</a></td><td colspan="2" style="background-color:light-dark(#eee, #27292d) !important;color:inherit;text-align:center"><a href="https://www.wikidata.org/wiki/Q14903574" class="extiw external" title="d:Q14903574">View/Edit Mouse</a></td></tr></tbody></table></td></tr></tbody></table>

<p><b>RAF proto-oncogene serine/threonine-protein kinase</b>, also known as <b>proto-oncogene c-RAF</b> or simply <b>c-Raf</b> or even <b>Raf-1</b>, is an <a href="Enzyme" title="Enzyme">enzyme</a><sup id="cite_ref-pmid1846778_4-0" class="reference"><a href="#cite_note-pmid1846778-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> that in humans is <a href="Genetic_code" title="Genetic code">encoded</a> by the <i>RAF1</i> <a href="Gene" title="Gene">gene</a>.<sup id="cite_ref-pmid6308607_5-0" class="reference"><a href="#cite_note-pmid6308607-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid6691137_6-0" class="reference"><a href="#cite_note-pmid6691137-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> The c-Raf protein is part of the <a href="MAPK/ERK_pathway" title="MAPK/ERK pathway">ERK1/2 pathway</a> as a MAP kinase (MAP3K) that functions downstream of the <a href="Ras_subfamily" class="mw-redirect" title="Ras subfamily">Ras subfamily</a> of membrane associated GTPases.<sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> C-Raf is a member of the <a href="Raf_kinase" class="mw-redirect" title="Raf kinase">Raf kinase</a> family of <a href="Serine/threonine-specific_protein_kinase" title="Serine/threonine-specific protein kinase">serine/threonine-specific protein kinases</a>, from the TKL (Tyrosine-kinase-like) group of kinases.

</p>

<div class="mw-heading mw-heading2"><h2 id="Discovery">Discovery</h2></div>

<p>The first Raf gene, <b>v-Raf</b> was found in 1983. It was isolated from the murine <a href="Retrovirus" title="Retrovirus">retrovirus</a> bearing the number 3611. It was soon demonstrated to be capable to transform rodent fibroblasts to cancerous <a href="Immortalised_cell_line" title="Immortalised cell line">cell lines</a>, so this gene was given the name Virus-induced Rapidly Accelerated Fibrosarcoma (V-RAF).<sup id="cite_ref-pmid6308607_5-1" class="reference"><a href="#cite_note-pmid6308607-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> A year later, another transforming gene was found in the avian retrovirus MH2, named v-Mil - that turned out to be highly similar to v-Raf.<sup id="cite_ref-pmid6325930_8-0" class="reference"><a href="#cite_note-pmid6325930-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> Researchers were able to demonstrate that these genes encode enzymes that have serine-threonine kinase activity.<sup id="cite_ref-pmid6438534_9-0" class="reference"><a href="#cite_note-pmid6438534-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> Normal cellular homologs of v-Raf and v-Mil were soon found in both the mouse and chicken genome (hence the name <b>c-Raf</b> for the normal <i>cellular</i> Raf gene), and it became clear that these too had a role in regulating growth and cell division.<sup id="cite_ref-pmid1992343_10-0" class="reference"><a href="#cite_note-pmid1992343-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid6324342_11-0" class="reference"><a href="#cite_note-pmid6324342-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup>

</p><p>c-Raf is a principal component of the <a href="Mitogen-activated_protein_kinase" title="Mitogen-activated protein kinase">mitogen-activated protein kinase</a> (MAPK) pathway: <a href="MAPK/ERK_pathway" title="MAPK/ERK pathway">ERK1/2 signaling</a>.<sup id="cite_ref-pmid1322500_12-0" class="reference"><a href="#cite_note-pmid1322500-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> It acts as a MAP3 kinase, initiating the entire kinase cascade. Subsequent experiments showed that the normal, cellular Raf genes can also mutate to become oncogenes, by "overdriving" MEK1/2 and ERK1/2 activity.<sup id="cite_ref-pmid2843497_13-0" class="reference"><a href="#cite_note-pmid2843497-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> In fact, vertebrate genomes contain multiple Raf genes. Several years later after the discovery of c-Raf, two further related kinases were described: <a href="ARAF" title="ARAF">A-Raf</a> and <a href="BRAF_(gene)" title="BRAF (gene)">B-Raf</a>. The latter became the focus of research in recent years, since a large portion of human tumors carry oncogenic 'driver' mutations in the B-Raf gene.<sup id="cite_ref-pmid12068308_14-0" class="reference"><a href="#cite_note-pmid12068308-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> These mutations induce an uncontrolled, high activity of Raf enzymes. Thus diagnostic and therapeutic interest in Raf kinases reached a new peak in the recent years.<sup id="cite_ref-pmid15827342_15-0" class="reference"><a href="#cite_note-pmid15827342-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup>

</p>

<div class="mw-heading mw-heading2"><h2 id="Structure">Structure</h2></div>

<p>The human c-Raf gene is located on <a href="Chromosome_3_(human)" class="mw-redirect" title="Chromosome 3 (human)">chromosome 3</a>. At least two isoforms of <a href="Messenger_RNA" title="Messenger RNA">mRNA</a> have been described (arising from inclusion or removal of an <a href="Alternative_splicing" title="Alternative splicing">alternative exon</a>) that display only minute differences. The shorter, major isoform - consisting of 17 <a href="Exon" title="Exon">exons</a> - encodes a <a href="Protein_kinase" title="Protein kinase">protein kinase</a> of 648 amino acids.<sup id="cite_ref-pmid1886707_16-0" class="reference"><a href="#cite_note-pmid1886707-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup>

</p>

<p>Similarly to many other <a href="MAP_kinase_kinase_kinase" title="MAP kinase kinase kinase">MAPKKKs</a>, c-Raf is a <a href="Protein_domain#Multidomain_proteins" title="Protein domain">multidomain protein</a>, with several additional <a href="Protein_domain" title="Protein domain">domains</a> to aid the regulation of its <a href="Enzyme" title="Enzyme">catalytic</a> activity. On its N-terminal segment, a Ras-binding domain (RBD) and a C-kinase homologous domain 1 (C1 domain) are found next to each other. Structures of both conserved domains were solved in the past decades, shedding light on the mechanisms of their regulation.

</p><p>The <a href="Raf-like_Ras-binding_domain" title="Raf-like Ras-binding domain">Ras-binding domain</a> displays a ubiquitin-like fold (like many other small G-protein associating domains) and selectively binds GTP-bound Ras proteins only.<sup id="cite_ref-pmid7791872_17-0" class="reference"><a href="#cite_note-pmid7791872-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid7766599_18-0" class="reference"><a href="#cite_note-pmid7766599-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid8503013_19-0" class="reference"><a href="#cite_note-pmid8503013-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> (You can see this interaction in high detail in the PDB box attached to the article. It shows Rap1 in complex with the RBD of c-Raf.)

</p><p>The <a href="C1_domain" title="C1 domain">C1 domain</a> - immediately downstream of the Ras binding domain - is a special <a href="Zinc_finger" title="Zinc finger">zinc finger</a>, rich in cysteines and stabilized by two zinc ions. It is similar to the diacylglycerol-binding C1 domains of <a href="Protein_kinase_C" title="Protein kinase C">protein kinase C</a> (PKC) enzymes.<sup id="cite_ref-pmid8710867_20-0" class="reference"><a href="#cite_note-pmid8710867-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid9774683_21-0" class="reference"><a href="#cite_note-pmid9774683-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> But unlike PKC, the C1 domains of Raf family kinases do not bind diacylglycerol.<sup id="cite_ref-pmid19710537_22-0" class="reference"><a href="#cite_note-pmid19710537-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> Instead, they interact with other lipids, such as ceramide<sup id="cite_ref-pmid19710537_22-1" class="reference"><a href="#cite_note-pmid19710537-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> or phosphatidic acid,<sup id="cite_ref-pmid18952605_23-0" class="reference"><a href="#cite_note-pmid18952605-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> and even aid in the recognition of activated Ras (GTP-Ras).<sup id="cite_ref-pmid9774683_21-1" class="reference"><a href="#cite_note-pmid9774683-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid7730360_24-0" class="reference"><a href="#cite_note-pmid7730360-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup>

</p><p>The close proximity of these two domains as well as several lines of experimental data suggest that they act as a single unit to negatively regulate the activity of the protein kinase domain, by direct physical interaction.<sup id="cite_ref-pmid9689060_25-0" class="reference"><a href="#cite_note-pmid9689060-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> Historically, this autoinhibitory block was labelled as the CR1 region ("Conserved Region 1"), the hinge region being named CR2, and the kinase domain CR3. Unfortunately, the precise structure of the autoinhibited kinase remains unknown.

</p><p>Between the autoinhibitory domain block and the catalytic kinase domain, a long segment - characteristic to all Raf proteins - can be found. It is highly enriched in <a href="Serine" title="Serine">serine</a> amino acids, but its precise <a href="Sequence_(biology)" title="Sequence (biology)">sequence</a> is poorly conserved across related Raf genes. This region appears to be intrinsically unstructured, and very flexible. Its most likely role is to act as a natural "hinge" between the rigidly folded autoinhibitory and catalytic domains, enabling complex movements and profound conformational rearrangements within the molecule.<sup id="cite_ref-pmid17074813_26-0" class="reference"><a href="#cite_note-pmid17074813-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> This hinge region contains a small, conserved <a href="Short_linear_motif" title="Short linear motif">island</a> of amino acids, that are responsible for <a href="14-3-3_protein" title="14-3-3 protein">14-3-3 protein</a> recognition, but only when a critical serine (Ser259 in human c-Raf) is phosphorylated. A second, similar motif is found on the extreme C-terminus (centered around the phosphorylatable Ser 621) of all Raf enzymes, but downstream of the kinase domain.

</p><p>The C-terminal half of c-Raf folds into a single protein domain, responsible for catalytic activity. The structure of this <a href="Protein_kinase_domain" title="Protein kinase domain">kinase domain</a> is well-known from both c-Raf<sup id="cite_ref-pmid20130576_27-0" class="reference"><a href="#cite_note-pmid20130576-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> and B-Raf.<sup id="cite_ref-pmid15035987_28-0" class="reference"><a href="#cite_note-pmid15035987-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> It is highly similar to other Raf kinases and KSR proteins, and distinctly similar to some other MAP3 kinases, such as the Mixed Lineage Kinase (MLK) family. Together they comprise the Tyrosine Kinase Like (TKL) group of protein kinases. Although some features unite their catalytic domains with protein tyrosine kinases, the activity of TKLs is restricted to the phosphorylation of serine and threonine residues within target proteins. The most important substrate of Raf kinases (apart from itself) are the <a href="MAP2K1" title="MAP2K1">MKK1</a> and <a href="MAP2K2" title="MAP2K2">MKK2</a> kinases, whose activity strictly depends on phosphorylation events performed by Rafs.

</p>

<div class="mw-heading mw-heading2"><h2 id="Evolutionary_relationships">Evolutionary relationships</h2></div>

<div role="note" class="hatnote navigation-not-searchable">Main article: <a href="Raf_kinase" class="mw-redirect" title="Raf kinase">Raf kinase</a></div>

<p>Human c-Raf is a member of a larger family of related protein kinases. Two further members - found in most vertebrates - belong to the same family: <a href="BRAF_(gene)" title="BRAF (gene)">B-Raf</a> and <a href="ARAF" title="ARAF">A-Raf</a>. Apart from the different length of their non-conserved N- and C-terminal ends, they all share the same domain architecture, structure and regulation. In comparison to the relatively well-known c-Raf and B-Raf, there is very little known of the precise function of A-Raf, but it is also thought to be similar to the other two members of the family. All these genes are believed to be the product of full gene or genome duplications at the dawn of vertebrate evolution, from a single ancestral Raf gene. Most other animal organisms possess only a single Raf gene. It is called Phl or Draf in Drosophila<sup id="cite_ref-pmid3037346_29-0" class="reference"><a href="#cite_note-pmid3037346-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> and Lin-45 in C. elegans.<sup id="cite_ref-pmid12639709_30-0" class="reference"><a href="#cite_note-pmid12639709-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup>

</p>

<p>Multicellular animals also have a type of kinase closely related to Raf: this is the Kinase Suppressor of Ras (KSR). Vertebrates like mammals have two, <a href="Homology_(biology)" title="Homology (biology)">paralogous</a> KSR genes instead of one: <a href="KSR1" title="KSR1">KSR1</a> and <a href="KSR2" title="KSR2">KSR2</a>. Their C-terminal kinase domain is very similar to Raf (originally called CA5 in KSR and CR3 in Raf), but the N-terminal regulatory region differs. Although they also have the flexible hinge (CA4 in KSR) and a C1 domain (CA3 in KSR) before it, KSRs entirely lack the Ras-binding domain. Instead, they have unique regulatory regions on their N-termini, originally termed CA1 ("conserved area 1") and CA2. For a long time, the structure of the CA1 domain was a mystery. However, in 2012, the structure of the CA1 region in KSR1 was solved: it turned out to be a divergent <a href="Sterile_alpha_motif" title="Sterile alpha motif">SAM</a> (sterile alpha motif) domain, supplemented with <a href="Coiled_coil" title="Coiled coil">coiled-coils</a> (CC-SAM): this is supposed to aid KSRs in membrane binding.<sup id="cite_ref-pmid23250398_31-0" class="reference"><a href="#cite_note-pmid23250398-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> KSRs, like Rafs, also have the twin 14-3-3 associating motifs (that depend on phosphorylation), but also possess novel MAPK-binding motifs on their hinge regions. With a typical sequence Phe-x-Phe-Pro (FxFP) these motifs are important for the feedback regulation of Raf kinases in the <a href="MAPK/ERK_pathway" title="MAPK/ERK pathway">ERK1/2 pathway</a>. According to our current knowledge, KSRs also participate in the same pathway as Raf, although they only play an auxiliary role. With a very poor intrinsic kinase activity, they were long thought to be inactive, until their catalytic activity was finally demonstrated in recent years.<sup id="cite_ref-pmid21441104_32-0" class="reference"><a href="#cite_note-pmid21441104-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid21441910_33-0" class="reference"><a href="#cite_note-pmid21441910-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> But even then, they contribute only negligibly to <a href="MAP2K1" title="MAP2K1">MKK1</a> and <a href="MAP2K2" title="MAP2K2">MKK2</a> phosphorylation. The main role of KSR appears to be to provide a heterodimerization partner to Raf enzymes, greatly facilitating their activation by means of allostery. Similar phenomena were described for other MAP3 kinases. ASK2, for example, is a poor enzyme on its own, and it activity appears to be tied to ASK1/ASK2 heterodimerisation.<sup id="cite_ref-pmid17714688_34-0" class="reference"><a href="#cite_note-pmid17714688-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup>

</p><p>Raf-like kinases are fully absent from fungi. But recent sequencing of other <a href="Opisthokont" title="Opisthokont">opisthokonts</a> (e.g. <a href="Capsaspora" title="Capsaspora">Capsaspora owczarzaki</a>) revealed the presence of genuine Raf kinases in unicellular eukaryotes. Therefore, it is possible that Raf proteins are an ancient heritage and ancestors of fungi secondarily lost Raf-dependent signaling. Fungal <a href="Mitogen-activated_protein_kinase" title="Mitogen-activated protein kinase">MAP kinase pathways</a> that are homologous to the mammalian <a href="MAPK/ERK_pathway" title="MAPK/ERK pathway">ERK1/2 pathway</a> (Fus3 and Kss1 in yeast) are activated by MEKK-related kinases (e.g. Ste11 in yeast) instead of Raf enzymes.

</p><p>Raf kinases found in retroviruses (such as murine v-Raf) are secondarily derived from the corresponding vertebrate genes of their hosts. These Raf genes encode severely truncated proteins, that lack the entire N-terminal autoinhibitory domain, and the 14-3-3 binding motifs. Such severe truncations are known to induce an uncontrolled activity of Raf kinases: that is just exactly what a virus may need for efficient reproduction.

</p>

<div class="mw-heading mw-heading2"><h2 id="Regulation_of_activity">Regulation of activity</h2></div>

<p>As mentioned above, the regulation of c-Raf activity is complex. As a "gatekeeper" of the <a href="MAPK/ERK_pathway" title="MAPK/ERK pathway">ERK1/2 pathway</a>, it is kept in check by a multitude of inhibitory mechanisms, and normally cannot be activated in a single step. The most important regulatory mechanism involves the direct, physical association of the N-terminal autoinhibitory block to the kinase domain of c-Raf. It results in the occlusion of the catalytic site and full shutdown of kinase activity.<sup id="cite_ref-pmid9689060_25-1" class="reference"><a href="#cite_note-pmid9689060-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> This "closed" state can only be relieved if the autoinhibitory domain of Raf engages a partner competing with its own kinase domain, most importantly GTP-bound Ras. Activated small G-proteins can thus break up the intramolecular interactions: this results in a conformational change ("opening") of c-Raf<sup id="cite_ref-pmid15711535_37-0" class="reference"><a href="#cite_note-pmid15711535-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup> necessary for kinase activation and substrate binding.

</p><p><a href="14-3-3_protein" title="14-3-3 protein">14-3-3 proteins</a> also contribute to the autoinhibition. As 14-3-3 proteins are all known to form constitutive dimers, their assemblies have two binding sites.<sup id="cite_ref-pmid7603574_38-0" class="reference"><a href="#cite_note-pmid7603574-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> Thus the dimer acts as a "molecular handcuff", locking their binding partners at a fixed distance and orientation. When the precisely positioned twin 14-3-3 binding motifs are engaged by a single 14-3-3 protein dimer (such as 14-3-3 zeta), they become locked into a conformation that promotes autoinhibition and does not allow the disengagement of the autoinhibitory and catalytic domains.<sup id="cite_ref-pmid19049963_39-0" class="reference"><a href="#cite_note-pmid19049963-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> This "lockdown" of c-Raf (and other Rafs as well as KSRs) is controlled by motif phosphorylation. Unphosphorylated 14-3-3 associating motifs do not bind their partners: they need to get phosphorylated on conserved serines (Ser 259 and Ser 621) first, by other protein kinases. The most important kinase implicated in this event is <a href="MAP3K7" title="MAP3K7">TGF-beta activated kinase 1</a> (TAK1), and the enzymes dedicated for removal of these phosphates are the <a href="Protein_phosphatase_1" title="Protein phosphatase 1">protein phosphatase 1</a> (PP1) and protein phosphatase 2A (PP2A) complexes.<sup id="cite_ref-pmid16630891_40-0" class="reference"><a href="#cite_note-pmid16630891-40"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid11494123_41-0" class="reference"><a href="#cite_note-pmid11494123-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup>

</p><p>Note that 14-3-3 binding of Raf enzymes is not necessarily inhibitory: once Raf is open and dimerizes, 14-3-3s can also bind in <i>trans</i>, bridging two kinases and "handcuffing" them together to reinforce the dimer, instead of keeping them away from each other.<sup id="cite_ref-pmid9665134_42-0" class="reference"><a href="#cite_note-pmid9665134-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup> Further modes of 14-3-3 interactions with c-Raf also exist, but their role is not well known.<sup id="cite_ref-pmid22922483_43-0" class="reference"><a href="#cite_note-pmid22922483-43"><span class="cite-bracket">[</span>43<span class="cite-bracket">]</span></a></sup>

</p><p>Dimerisation is another important mechanism for c-Raf activity regulation and required for Raf <a href="Activation_loop" class="mw-redirect" title="Activation loop">activation loop</a> phosphorylation. Normally, only the "open" kinase domains participate in dimerisation. Unlike B-Raf, that readily forms homodimers with itself, c-Raf prefers heterodimerisation with either B-Raf or KSR1. Homodimers and heterodimers all behave similarly.<sup id="cite_ref-pmid21441910_33-1" class="reference"><a href="#cite_note-pmid21441910-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> The B-Raf homodimer kinase domain structure clearly shows that the activation loops (that control the catalytic activity of all known protein kinases) are positioned in an active-like conformation in the dimer. This is due to an allosteric effect of the other molecule binding to the "back" side of the kinase; such dimers are symmetric and have two, partially active catalytic sites. At this stage, the activity of Raf kinases is low, and unstable.

</p>

<p>To achieve full activity and stabilize the active state, the activation loop of c-Raf needs to be phosphorylated. The only kinases currently known to perform this act are the Raf family kinases themselves. But some other kinases, such as PAK1 can phosphorylate other residues near the kinase domain of c-Raf: the precise role of these auxiliary kinases is unknown. In the context of c-Raf, both c-Raf and KSR1 are needed for the "transphosphorylation" step. Due to the architecture of the dimers, this phosphorylation can only take place in <i>trans</i> (i.e. one dimer phosphorylates another, in a four-membered transitional complex).<sup id="cite_ref-pmid22292131_44-0" class="reference"><a href="#cite_note-pmid22292131-44"><span class="cite-bracket">[</span>44<span class="cite-bracket">]</span></a></sup> By interacting with conserved Arg and Lys residues in the kinase domain, the phosphorylated activation loops shift conformation and become ordered, permanently locking the kinase domain into a fully active state until dephosphorylated. The phosphorylated activation loops also render the kinase insensitive to the presence of its autoinhibitory domain.<sup id="cite_ref-pmid12865432_45-0" class="reference"><a href="#cite_note-pmid12865432-45"><span class="cite-bracket">[</span>45<span class="cite-bracket">]</span></a></sup> KSRs cannot undergo this last step as they miss any phosphorylatable residues in their activation loops. But once c-Raf is fully activated, there is no further need to do so: active Raf enzymes can now engage their substrates.<sup id="cite_ref-pmid21617065_46-0" class="reference"><a href="#cite_note-pmid21617065-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup> Like most protein kinases, c-Raf has multiple substrates. <a href="Bcl-2-associated_death_promoter" title="Bcl-2-associated death promoter">BAD</a> (Bcl2-atagonist of cell death) is directly phosphorylated by c-Raf,<sup id="cite_ref-pmid22096607_47-0" class="reference"><a href="#cite_note-pmid22096607-47"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup> along with several types of <a href="Adenylate_cyclase" class="mw-redirect" title="Adenylate cyclase">adenylate cyclases</a>,<sup id="cite_ref-pmid15385642_48-0" class="reference"><a href="#cite_note-pmid15385642-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup> <a href="(myosin-light-chain)_phosphatase" class="mw-redirect" title="(myosin-light-chain) phosphatase">myosin phosphatase</a> (MYPT),<sup id="cite_ref-pmid11719507_49-0" class="reference"><a href="#cite_note-pmid11719507-49"><span class="cite-bracket">[</span>49<span class="cite-bracket">]</span></a></sup> <a href="Troponin" title="Troponin">cardiac muscle troponin T</a> (TnTc),<sup id="cite_ref-pmid19381846_50-0" class="reference"><a href="#cite_note-pmid19381846-50"><span class="cite-bracket">[</span>50<span class="cite-bracket">]</span></a></sup> etc. The <a href="Retinoblastoma_protein" title="Retinoblastoma protein">retinoblastoma protein</a> (pRb) and <a href="Cdc25" title="Cdc25">Cdc25 phosphatase</a> were also suggested as possible substrates.<sup id="cite_ref-pmid11950876_51-0" class="reference"><a href="#cite_note-pmid11950876-51"><span class="cite-bracket">[</span>51<span class="cite-bracket">]</span></a></sup>

</p><p>The most important targets of all Raf enzymes are <a href="MAP2K1" title="MAP2K1">MKK1(MEK1)</a> and <a href="MAP2K2" title="MAP2K2">MKK2(MEK2)</a>. Although the structure of the enzyme-substrate complex c-Raf:MKK1 is unknown, it can be precisely modelled after the KSR2:MKK1 complex.<sup id="cite_ref-pmid21441910_33-2" class="reference"><a href="#cite_note-pmid21441910-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> Here no actual catalysis takes place, but it is thought to be highly similar to the way Raf binds to its substrates. The main interaction interface is provided by the C-terminal lobes of both kinase domains; the large, disordered, proline-rich loop unique to <a href="MAP2K1" title="MAP2K1">MKK1</a> and <a href="MAP2K2" title="MAP2K2">MKK2</a> also plays an important role in its positioning to Raf (and KSR).<sup id="cite_ref-pmid7565670_52-0" class="reference"><a href="#cite_note-pmid7565670-52"><span class="cite-bracket">[</span>52<span class="cite-bracket">]</span></a></sup> These MKKs become phosphorylated on at least two sites in their activation loops upon binding to Raf: this will activate them too. The targets of the kinase cascade are ERK1 and ERK2, that are selectively activated by MKK1 or MKK2. ERKs have numerous substrates in cells; they are also capable of translocating into the nucleus to activate nuclear transcription factors. Activated ERKs are pleiotropic effectors of cell physiology and play an important role in the control of gene expression involved in the cell division cycle, cell migration, inhibition of apoptosis, and cell differentiation.

</p>

<div class="mw-heading mw-heading2"><h2 id="Associated_human_diseases">Associated human diseases</h2></div>

<p>Hereditary gain-of-function mutations of c-Raf are implicated in some rare, but severe syndromes. Most of these mutations involve single amino acid changes at one of the two 14-3-3 binding motifs.<sup id="cite_ref-pmid17603483_53-0" class="reference"><a href="#cite_note-pmid17603483-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid20679480_54-0" class="reference"><a href="#cite_note-pmid20679480-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup> Mutation of c-Raf is one of the possible causes of <a href="Noonan_syndrome" title="Noonan syndrome">Noonan syndrome</a>: affected individuals have congenital heart defects, short and dysmorphic stature and several other deformities. Similar mutations in c-Raf can also cause a related condition, termed <a href="LEOPARD_syndrome" class="mw-redirect" title="LEOPARD syndrome">LEOPARD syndrome</a> (Lentigo, Electrocardiographic abnormalities, Ocular hypertelorism, Pulmonary stenosis, Abnormal genitalia, Retarded growth, Deafness), with a complex association of defects.

</p>

<div class="mw-heading mw-heading2"><h2 id="Role_in_cancer">Role in cancer</h2></div>

<p>Although c-Raf is very clearly capable of mutating into an oncogene in experimental settings, and even in a few human tumors,<sup id="cite_ref-pmid8451761_55-0" class="reference"><a href="#cite_note-pmid8451761-55"><span class="cite-bracket">[</span>55<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid16585161_56-0" class="reference"><a href="#cite_note-pmid16585161-56"><span class="cite-bracket">[</span>56<span class="cite-bracket">]</span></a></sup> its sister kinase B-Raf is the true major player in carcinogenesis in humans.<sup id="cite_ref-pmid16266992_57-0" class="reference"><a href="#cite_note-pmid16266992-57"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup>

</p>

<div class="mw-heading mw-heading3"><h3 id="B-Raf_mutations">B-Raf mutations</h3></div>

<p>Approximately 20% of all examined human tumor samples display a mutated B-Raf gene.<sup id="cite_ref-pmid20952405_58-0" class="reference"><a href="#cite_note-pmid20952405-58"><span class="cite-bracket">[</span>58<span class="cite-bracket">]</span></a></sup> The overwhelming majority of these mutations involve the exchange of a single amino acid: Val 600 into Glu, and this aberrant gene product (BRAF-V600E) can be visualized by immunohistochemistry for clinical molecular diagnostics<sup id="cite_ref-pmid22012135_59-0" class="reference"><a href="#cite_note-pmid22012135-59"><span class="cite-bracket">[</span>59<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid21638088_60-0" class="reference"><a href="#cite_note-pmid21638088-60"><span class="cite-bracket">[</span>60<span class="cite-bracket">]</span></a></sup> The aberration can mimic the activation loop phosphorylation and - by jumping all control steps at normal activation - immediately render the kinase domain fully active.<sup id="cite_ref-pmid15710605_61-0" class="reference"><a href="#cite_note-pmid15710605-61"><span class="cite-bracket">[</span>61<span class="cite-bracket">]</span></a></sup> Since B-Raf can also activate itself by homodimerisation and c-Raf by heterodimerisation, this mutation has a catastrophic effect by turning the ERK1/2 pathway constitutively active, and driving an uncontrolled process of cell division.<sup id="cite_ref-pmid16364920_62-0" class="reference"><a href="#cite_note-pmid16364920-62"><span class="cite-bracket">[</span>62<span class="cite-bracket">]</span></a></sup>

</p>

<div class="mw-heading mw-heading2"><h2 id="As_a_therapeutic_target">As a therapeutic target</h2></div>

<p>Due to the importance of both Ras and B-Raf mutations in tumorigenesis, several Raf inhibitors were developed to combat cancer, especially against B-Raf exhibiting the V600E mutation. <a href="Sorafenib" title="Sorafenib">Sorafenib</a> was the first clinically useful agent, that provides a pharmacological alternative to treat previously largely untreatable malignancies, such as renal cell carcinoma and melanoma.<sup id="cite_ref-pmid21577205_63-0" class="reference"><a href="#cite_note-pmid21577205-63"><span class="cite-bracket">[</span>63<span class="cite-bracket">]</span></a></sup> Several other molecules followed up, such as <a href="Vemurafenib" title="Vemurafenib">Vemurafenib</a>, <a href="Regorafenib" title="Regorafenib">Regorafenib</a>, <a href="Dabrafenib" title="Dabrafenib">Dabrafenib</a>, etc.

</p><p>Unfortunately, ATP-competitive <a href="B-Raf_inhibitor" class="mw-redirect" title="B-Raf inhibitor">B-Raf inhibitors</a> may have an undesired effect in K-Ras-dependent cancers: They are simply too selective for B-Raf. While they perfectly well inhibit B-Raf activity in case a mutant B-Raf is the primary culprit, they also promote homo- and heterodimerisation of B-Raf, with itself and c-Raf. This will actually <i>enhance</i> c-Raf activation instead of inhibiting it in case there is no mutation in any Raf genes, but their common upstream activator K-Ras protein is the one mutated.<sup id="cite_ref-pmid20130576_27-1" class="reference"><a href="#cite_note-pmid20130576-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> This "paradoxical" c-Raf activation necessitates the need to screen for B-Raf mutations in patients (by genetic diagnostics) before starting a B-Raf-inhibitor therapy.<sup id="cite_ref-pmid22553052_64-0" class="reference"><a href="#cite_note-pmid22553052-64"><span class="cite-bracket">[</span>64<span class="cite-bracket">]</span></a></sup>

</p>

<div class="mw-heading mw-heading2"><h2 id="List_of_interacting_proteins">List of interacting proteins</h2></div>

<p>C-Raf has been shown to <a href="Protein-protein_interaction" class="mw-redirect" title="Protein-protein interaction">interact</a> with:

</p>

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<li><a href="CFLAR" title="CFLAR">CFLAR</a>,<sup id="cite_ref-pmid10837247_72-0" class="reference"><a href="#cite_note-pmid10837247-72"><span class="cite-bracket">[</span>72<span class="cite-bracket">]</span></a></sup></li>

<li><a href="Protein_kinase_M%CE%B6" class="mw-redirect" title="Protein kinase Mζ">PRKCZ</a>,<sup id="cite_ref-pmid10620507_102-0" class="reference"><a href="#cite_note-pmid10620507-102"><span class="cite-bracket">[</span>102<span class="cite-bracket">]</span></a></sup></li>

<li><a href="YWHAB" title="YWHAB">YWHAB</a>,<sup id="cite_ref-pmid12620389_80-1" class="reference"><a href="#cite_note-pmid12620389-80"><span class="cite-bracket">[</span>80<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid10620507_102-1" class="reference"><a href="#cite_note-pmid10620507-102"><span class="cite-bracket">[</span>102<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid12360521_111-0" class="reference"><a href="#cite_note-pmid12360521-111"><span class="cite-bracket">[</span>111<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid10848612_112-0" class="reference"><a href="#cite_note-pmid10848612-112"><span class="cite-bracket">[</span>112<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid8702721_113-0" class="reference"><a href="#cite_note-pmid8702721-113"><span class="cite-bracket">[</span>113<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid7644510_114-0" class="reference"><a href="#cite_note-pmid7644510-114"><span class="cite-bracket">[</span>114<span class="cite-bracket">]</span></a></sup></li>

<li><a href="YWHAE" title="YWHAE">YWHAE</a>,<sup id="cite_ref-pmid8702721_113-1" class="reference"><a href="#cite_note-pmid8702721-113"><span class="cite-bracket">[</span>113<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid7644510_114-1" class="reference"><a href="#cite_note-pmid7644510-114"><span class="cite-bracket">[</span>114<span class="cite-bracket">]</span></a></sup></li>

<li><a href="YWHAG" title="YWHAG">YWHAG</a>,<sup id="cite_ref-pmid10620507_102-2" class="reference"><a href="#cite_note-pmid10620507-102"><span class="cite-bracket">[</span>102<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid17353931_115-0" class="reference"><a href="#cite_note-pmid17353931-115"><span class="cite-bracket">[</span>115<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid10433554_116-0" class="reference"><a href="#cite_note-pmid10433554-116"><span class="cite-bracket">[</span>116<span class="cite-bracket">]</span></a></sup></li>

<li><a href="YWHAH" title="YWHAH">YWHAH</a>,<sup id="cite_ref-pmid10620507_102-3" class="reference"><a href="#cite_note-pmid10620507-102"><span class="cite-bracket">[</span>102<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid8702721_113-2" class="reference"><a href="#cite_note-pmid8702721-113"><span class="cite-bracket">[</span>113<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid11969417_117-0" class="reference"><a href="#cite_note-pmid11969417-117"><span class="cite-bracket">[</span>117<span class="cite-bracket">]</span></a></sup></li>

<li><a href="YWHAQ" title="YWHAQ">YWHAQ</a>,<sup id="cite_ref-pmid10757792_95-2" class="reference"><a href="#cite_note-pmid10757792-95"><span class="cite-bracket">[</span>95<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid10620507_102-4" class="reference"><a href="#cite_note-pmid10620507-102"><span class="cite-bracket">[</span>102<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid17353931_115-1" class="reference"><a href="#cite_note-pmid17353931-115"><span class="cite-bracket">[</span>115<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid8663231_118-0" class="reference"><a href="#cite_note-pmid8663231-118"><span class="cite-bracket">[</span>118<span class="cite-bracket">]</span></a></sup> and</li>

<li><a href="YWHAZ" title="YWHAZ">YWHAZ</a>.<sup id="cite_ref-pmid10620507_102-5" class="reference"><a href="#cite_note-pmid10620507-102"><span class="cite-bracket">[</span>102<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid9261098_119-0" class="reference"><a href="#cite_note-pmid9261098-119"><span class="cite-bracket">[</span>119<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid10887173_120-0" class="reference"><a href="#cite_note-pmid10887173-120"><span class="cite-bracket">[</span>120<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid7628630_121-0" class="reference"><a href="#cite_note-pmid7628630-121"><span class="cite-bracket">[</span>121<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid10611249_122-0" class="reference"><a href="#cite_note-pmid10611249-122"><span class="cite-bracket">[</span>122<span class="cite-bracket">]</span></a></sup></li></ul>

</div>

<ul><li><a href="Raf_kinase" class="mw-redirect" title="Raf kinase">Raf kinases</a></li>

<li><a href="ARAF" title="ARAF">A-Raf kinase</a></li>

<li><a href="BRAF_(gene)" title="BRAF (gene)">B-Raf kinase</a></li>

<li><a href="KSR1" title="KSR1">KSR1 protein</a></li>

<li><a href="KSR2" title="KSR2">KSR2 protein</a></li></ul>

<div class="mw-heading mw-heading2"><h2 id="References">References</h2></div>

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<li id="cite_note-pmid10887173-120"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid10887173_120-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFTzivionLuoAvruch2000" class="citation journal cs1">Tzivion G, Luo ZJ, Avruch J (September 2000). <a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M001207200">"Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo"</a>. <i>J. Biol. Chem</i>. <b>275</b> (38): <span class="nowrap">29772–</span>8. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M001207200">10.1074/jbc.M001207200</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10887173">10887173</a>.</cite></span>

</li>

<li id="cite_note-pmid7628630-121"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid7628630_121-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFKoyamaWilliamsKikuchi1995" class="citation journal cs1">Koyama S, Williams LT, Kikuchi A (July 1995). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0014-5793%2895%2900686-4">"Characterization of the interaction of Raf-1 with ras p21 or 14-3-3 protein in intact cells"</a>. <i>FEBS Lett</i>. <b>368</b> (2): <span class="nowrap">321–</span>5. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1995FEBSL.368..321K">1995FEBSL.368..321K</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0014-5793%2895%2900686-4">10.1016/0014-5793(95)00686-4</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/7628630">7628630</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:29625141">29625141</a>.</cite></span>

</li>

<li id="cite_note-pmid10611249-122"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid10611249_122-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFChowDavis2000" class="citation journal cs1">Chow CW, Davis RJ (January 2000). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC85175">"Integration of calcium and cyclic AMP signaling pathways by 14-3-3"</a>. <i>Mol. Cell. Biol</i>. <b>20</b> (2): <span class="nowrap">702–</span>12. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1128%2FMCB.20.2.702-712.2000">10.1128/MCB.20.2.702-712.2000</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC85175">85175</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10611249">10611249</a>.</cite></span>

</li>

</ol></div>

<div class="mw-heading mw-heading2"><h2 id="Further_reading">Further reading</h2></div>

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<ul><li><cite id="CITEREFReedZhaAime-SempeTakayama1996" class="citation book cs1">Reed JC, Zha H, Aime-Sempe C, Takayama S, Wang HG (1996). "Structure—Function Analysis of BCL-2 Family Proteins". <i>Mechanisms of Lymphocyte Activation and Immune Regulation VI</i>. Adv. Exp. Med. Biol. Vol. 406. pp. <span class="nowrap">99–</span>112. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2F978-1-4899-0274-0_10">10.1007/978-1-4899-0274-0_10</a>. <a href="ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <bdi>978-1-4899-0276-4</bdi>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/8910675">8910675</a>.</cite></li>

<li><cite id="CITEREFGeyerFacklerPeterlin2001" class="citation journal cs1">Geyer M, Fackler OT, Peterlin BM (2001). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1083955">"Structure–function relationships in HIV-1 Nef"</a>. <i>EMBO Rep</i>. <b>2</b> (7): <span class="nowrap">580–</span>5. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1093%2Fembo-reports%2Fkve141">10.1093/embo-reports/kve141</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1083955">1083955</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11463741">11463741</a>.</cite></li>

<li><cite id="CITEREFDhillonKolch2002" class="citation journal cs1">Dhillon AS, Kolch W (2002). "Untying the regulation of the Raf-1 kinase". <i>Arch. Biochem. Biophys</i>. <b>404</b> (1): <span class="nowrap">3–</span>9. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0003-9861%2802%2900244-8">10.1016/S0003-9861(02)00244-8</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12127063">12127063</a>.</cite></li>

<li><cite id="CITEREFGreenwayHollowayMcPheeEllis2004" class="citation journal cs1">Greenway AL, Holloway G, McPhee DA, Ellis P, Cornall A, Lidman M (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication". <i>J. Biosci</i>. <b>28</b> (3): <span class="nowrap">323–</span>35. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2FBF02970151">10.1007/BF02970151</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12734410">12734410</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:33749514">33749514</a>.</cite></li>

<li><cite id="CITEREFChenKunnimalaiyaanVan_Gompel2006" class="citation journal cs1">Chen H, Kunnimalaiyaan M, Van Gompel JJ (2006). "Medullary thyroid cancer: the functions of raf-1 and human achaete-scute homologue-1". <i>Thyroid</i>. <b>15</b> (6): <span class="nowrap">511–</span>21. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1089%2Fthy.2005.15.511">10.1089/thy.2005.15.511</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16029117">16029117</a>.</cite></li></ul>

</div>

<div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2></div>

<ul><li><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/NBK1124/">GeneReviews/NCBI/NIH/UW entry on Noonan syndrome</a></li>

<li>Domain structure <a rel="nofollow" class="external text" href="http://www.ebi.ac.uk/interpro/ISpy?ipr=IPR003116&tax_id=9606">diagrams</a> for Raf-1, A-Raf and B-Raf.</li>

<li><a rel="nofollow" class="external text" href="http://www.sdbonline.org/fly/genebrief/raf.htm"><i>Drosophila</i> <i>pole hole</i> - The Interactive Fly</a></li>

<li><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=c-raf+Proteins">c-raf+Proteins</a> at the U.S. National Library of Medicine <a href="Medical_Subject_Headings" title="Medical Subject Headings">Medical Subject Headings</a> (MeSH)</li>

<li>Human <a rel="nofollow" class="external text" href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=RAF1"><i>RAF1</i></a> genome location and <a rel="nofollow" class="external text" href="https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=RAF1"><i>RAF1</i></a> gene details page in the <a href="UCSC_Genome_Browser" title="UCSC Genome Browser">UCSC Genome Browser</a>.</li>

<li>Overview of all the structural information available in the <a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a> for <a href="UniProt" title="UniProt">UniProt</a>: <i><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P04049">P04049</a></i> (RAF proto-oncogene serine/threonine-protein kinase) at the <a href="PDBe-KB" title="PDBe-KB">PDBe-KB</a>.</li></ul>

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<div class="gallerytext"><b>1c1y</b>: CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).</div>

</li>

<div class="gallerytext"><b>1faq</b>: RAF-1 CYSTEINE RICH DOMAIN, NMR, 27 STRUCTURES</div>

</li>

<div class="gallerytext"><b>1far</b>: RAF-1 CYSTEINE RICH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE</div>

</li>

<div class="gallerytext"><b>1gua</b>: HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131</div>

</li>

<div class="gallerytext"><b>1rfa</b>: NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1</div>

</li>

</ul></div></td></tr></tbody></table></div>

<div class="navbox-styles"></div><div role="navigation" class="navbox" aria-labelledby="Signaling_pathway:_MAPK/ERK_pathway136" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2" style="background:#e7dcc3"><div id="Signaling_pathway:_MAPK/ERK_pathway136" style="font-size:114%;margin:0 4em"><a href="Signal_transduction" title="Signal transduction">Signaling pathway</a>: <a href="MAPK/ERK_pathway" title="MAPK/ERK pathway">MAPK/ERK pathway</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Ligand_(biochemistry)" title="Ligand (biochemistry)">Ligand</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Epidermal_growth_factor" title="Epidermal growth factor">Epidermal growth factor</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="Receptor_(biochemistry)" title="Receptor (biochemistry)">Receptor</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Epidermal_growth_factor_receptor" title="Epidermal growth factor receptor">Epidermal growth factor receptor</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite">Other</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table></div>

<div class="navbox-styles"></div><div role="navigation" class="navbox" aria-labelledby="Tumor_suppressor_genes_and_Oncogenes246" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Tumor_suppressor_genes_and_Oncogenes246" style="font-size:114%;margin:0 4em"><a href="Tumor_suppressor_gene" title="Tumor suppressor gene">Tumor suppressor genes</a> and <a href="Oncogene" title="Oncogene">Oncogenes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Ligand_(biochemistry)" title="Ligand (biochemistry)">Ligand</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="Growth_factors18" scope="row" class="navbox-group" style="width:1%"><a href="Growth_factor" title="Growth factor">Growth factors</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="ONCO4" scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Receptor_(biochemistry)" title="Receptor (biochemistry)">Receptor</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Wnt_signaling_pathway" title="Wnt signaling pathway">Wnt signaling pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="TSP3" scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Hedgehog_signaling_pathway" title="Hedgehog signaling pathway">Hedgehog signaling pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="TSP3" scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="TGF_beta_signaling_pathway" title="TGF beta signaling pathway">TGF beta signaling pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="TSP3" scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="TGF_beta_receptor_2" title="TGF beta receptor 2">TGF beta receptor 2</a></li></ul>

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Receptor_tyrosine_kinase" title="Receptor tyrosine kinase">Receptor tyrosine kinase</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="ONCO4" scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="JAK-STAT_signaling_pathway" title="JAK-STAT signaling pathway">JAK-STAT signaling pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="ONCO4" scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Intracellular_signaling_peptides_and_proteins" class="mw-redirect" title="Intracellular signaling peptides and proteins">Intracellular signaling P+Ps</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Wnt_signaling_pathway" title="Wnt signaling pathway">Wnt signaling pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Beta-catenin" class="mw-redirect" title="Beta-catenin">Beta-catenin</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="TGF_beta_signaling_pathway" title="TGF beta signaling pathway">TGF beta signaling pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="TSP3" scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Akt/PKB_signaling_pathway" title="Akt/PKB signaling pathway">Akt/PKB signaling pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Hippo_signaling_pathway" title="Hippo signaling pathway">Hippo signaling pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="TSP3" scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Merlin_(protein)" title="Merlin (protein)">Neurofibromin 2/Merlin</a></li></ul>

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="MAPK/ERK_pathway" title="MAPK/ERK pathway">MAPK/ERK pathway</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</ul>

<ul><li><a href="Neurofibromin" title="Neurofibromin">Neurofibromin 1</a></li></ul>

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other/unknown</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Maspin" title="Maspin">Maspin</a></li></ul>

</div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Cell_nucleus" title="Cell nucleus">Nucleus</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Cell_cycle" title="Cell cycle">Cell cycle</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<li><a href="Cyclin_D" title="Cyclin D">Cyclin D</a></li>

<li><a href="Cyclin_E" title="Cyclin E">Cyclin E</a></li></ul>

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="DNA_repair" title="DNA repair">DNA repair</a>/<a href="Fanconi_anemia" title="Fanconi anemia">Fanconi</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="TSP3" scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Ubiquitin_ligase" title="Ubiquitin ligase">Ubiquitin ligase</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Transcription_factor" title="Transcription factor">Transcription factor</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">ONCO</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">TSP</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Mitochondrion" title="Mitochondrion">Mitochondrion</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="Apoptosis_inhibitor46" scope="row" class="navbox-group" style="width:1%"><a href="Inhibitor_of_apoptosis" title="Inhibitor of apoptosis">Apoptosis inhibitor</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other/ungrouped</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<li><a href="Notch_signaling" class="mw-redirect" title="Notch signaling">Notch</a></li>

<li><a href="Stathmin" title="Stathmin">Stathmin</a></li></ul>

</div></td></tr></tbody></table></div>

<div class="navbox-styles"></div><div role="navigation" class="navbox" aria-labelledby="Kinases:_Serine/threonine-specific_protein_kinases_(EC_2.7.11-12)102" style="padding:3px"><table class="nowraplinks mw-collapsible mw-collapsed navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Kinases:_Serine/threonine-specific_protein_kinases_(EC_2.7.11-12)102" style="font-size:114%;margin:0 4em"><a href="Kinase" title="Kinase">Kinases</a>: <a href="Serine/threonine-specific_protein_kinase" title="Serine/threonine-specific protein kinase">Serine/threonine-specific protein kinases</a> (<a href="Enzyme_Commission_number" title="Enzyme Commission number">EC</a> 2.7.11-12)</div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks mw-collapsible mw-collapsed navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Serine/threonine-specific_protein_kinases_(EC_2.7.11.1-EC_2.7.11.20)102" style="font-size:114%;margin:0 4em"><a href="Serine/threonine-specific_protein_kinase" title="Serine/threonine-specific protein kinase">Serine/threonine-specific protein kinases</a> (EC 2.7.11.1-EC 2.7.11.20)</div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Non-specific_serine/threonine_protein_kinase" class="mw-redirect" title="Non-specific serine/threonine protein kinase">Non-specific serine/threonine protein kinases</a> (EC 2.7.11.1)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<li><a href="AKT" class="mw-redirect" title="AKT">Protein kinase B</a>

<li><a href="Ataxia_telangiectasia_mutated" class="mw-redirect" title="Ataxia telangiectasia mutated">Ataxia telangiectasia mutated</a></li>

<li><a href="EIF-2_kinase" title="EIF-2 kinase">EIF-2 kinases</a>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Pyruvate_dehydrogenase_kinase" title="Pyruvate dehydrogenase kinase">Pyruvate dehydrogenase kinase</a> (EC 2.7.11.2)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Dephospho-(reductase_kinase)_kinase" title="Dephospho-(reductase kinase) kinase">Dephospho-(reductase kinase) kinase</a> (EC 2.7.11.3)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="AMP-activated_protein_kinase" title="AMP-activated protein kinase">AMP-activated protein kinase</a> α

<ul><li><a href="Protein_kinase%2C_AMP-activated%2C_alpha_1" title="Protein kinase, AMP-activated, alpha 1">PRKAA1</a></li>

<li><a href="PRKAA2" title="PRKAA2">PRKAA2</a></li></ul></li>

<li>β

<ul><li><a href="PRKAB1" title="PRKAB1">PRKAB1</a></li>

<li><a href="PRKAB2" title="PRKAB2">PRKAB2</a></li></ul></li>

<li>γ

<ul><li><a href="PRKAG1" title="PRKAG1">PRKAG1</a></li>

<li><a href="PRKAG2" title="PRKAG2">PRKAG2</a></li>

<li><a href="PRKAG3" title="PRKAG3">PRKAG3</a></li></ul></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="3-methyl-2-oxobutanoate_dehydrogenase_(acetyl-transferring)_kinase" title="3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase">3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase</a> (EC 2.7.11.4)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="BCKDK" title="BCKDK">BCKDK</a></li>

<li><a href="BCKDHA" title="BCKDHA">BCKDHA</a></li>

<li><a href="BCKDHB" title="BCKDHB">BCKDHB</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="(isocitrate_dehydrogenase_(NADP%2B))_kinase" class="mw-redirect" title="(isocitrate dehydrogenase (NADP+)) kinase">(isocitrate dehydrogenase (NADP+)) kinase</a> (EC 2.7.11.5)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="(tyrosine_3-monooxygenase)_kinase" title="(tyrosine 3-monooxygenase) kinase">(tyrosine 3-monooxygenase) kinase</a> (EC 2.7.11.6)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Myosin-heavy-chain_kinase" title="Myosin-heavy-chain kinase">Myosin-heavy-chain kinase</a> (EC 2.7.11.7)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Aurora_kinase" title="Aurora kinase">Aurora kinase</a>

<ul><li><a href="Aurora_A_kinase" class="mw-redirect" title="Aurora A kinase">Aurora A kinase</a></li>

<li><a href="Aurora_B_kinase" class="mw-redirect" title="Aurora B kinase">Aurora B kinase</a></li>

<li><a href="Aurora_C_kinase" class="mw-redirect" title="Aurora C kinase">Aurora C kinase</a></li></ul></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Fas-activated_serine/threonine_kinase" title="Fas-activated serine/threonine kinase">Fas-activated serine/threonine kinase</a> (EC 2.7.11.8)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="FASTK" title="FASTK">FASTK</a></li>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Goodpasture-antigen-binding_protein_kinase" title="Goodpasture-antigen-binding protein kinase">Goodpasture-antigen-binding protein kinase</a> (EC 2.7.11.9)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="I%CE%BAB_kinase" title="IκB kinase">IκB kinase</a> (EC 2.7.11.10)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<li><a href="IKBKE" title="IKBKE">IKBKE</a></li>

<li><a href="IKBKG" title="IKBKG">IKBKG</a></li>

<li><a href="IKBKAP" title="IKBKAP">IKBKAP</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Protein_kinase_A" title="Protein kinase A">cAMP-dependent protein kinase</a> (EC 2.7.11.11)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Protein_kinase_A" title="Protein kinase A">Protein kinase A</a></li>

<li><a href="PRKACG" title="PRKACG">PRKACG</a></li>

<li><a href="PRKACB" title="PRKACB">PRKACB</a></li>

<li><a href="PRKACA" title="PRKACA">PRKACA</a></li>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="CGMP-dependent_protein_kinase" title="CGMP-dependent protein kinase">cGMP-dependent protein kinase</a> (EC 2.7.11.12)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="CGMP-dependent_protein_kinase" title="CGMP-dependent protein kinase">Protein kinase G</a></li>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Protein_kinase_C" title="Protein kinase C">Protein kinase C</a> (EC 2.7.11.13)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Protein_kinase_C" title="Protein kinase C">Protein kinase C</a></li>

<li><a href="Protein_kinase_C_zeta_type" title="Protein kinase C zeta type">Protein kinase Cζ</a></li>

<li><a href="PKC_alpha" title="PKC alpha">PKC alpha</a></li>

<li><a href="PRKCB1" title="PRKCB1">PRKCB1</a></li>

<li><a href="PRKCD" title="PRKCD">PRKCD</a></li>

<li><a href="PRKCE" title="PRKCE">PRKCE</a></li>

<li><a href="PRKCH" title="PRKCH">PRKCH</a></li>

<li><a href="PRKCG" title="PRKCG">PRKCG</a></li>

<li><a href="PRKCI" title="PRKCI">PRKCI</a></li>

<li><a href="PRKCQ" title="PRKCQ">PRKCQ</a></li>

<li><a href="Protein_kinase_N1" title="Protein kinase N1">Protein kinase N1</a></li>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Rhodopsin_kinase" title="Rhodopsin kinase">Rhodopsin kinase</a> (EC 2.7.11.14)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Rhodopsin_kinase" title="Rhodopsin kinase">Rhodopsin kinase</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Beta_adrenergic_receptor_kinase" class="mw-redirect" title="Beta adrenergic receptor kinase">Beta adrenergic receptor kinase</a> (EC 2.7.11.15)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Beta_adrenergic_receptor_kinase" class="mw-redirect" title="Beta adrenergic receptor kinase">Beta adrenergic receptor kinase</a></li>

<li><a href="Beta_adrenergic_receptor_kinase-2" class="mw-redirect" title="Beta adrenergic receptor kinase-2">Beta adrenergic receptor kinase-2</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="G_protein-coupled_receptor_kinase" title="G protein-coupled receptor kinase">G-protein coupled receptor kinases</a> (EC 2.7.11.16)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Ca2%2B/calmodulin-dependent_protein_kinase" class="mw-redirect" title="Ca2+/calmodulin-dependent protein kinase">Ca2+/calmodulin-dependent</a> (EC 2.7.11.17)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<li><a href="MAPKAPK2" title="MAPKAPK2">MAPKAPK2</a></li>

<li><a href="MAPKAPK3" title="MAPKAPK3">MAPKAPK3</a></li>

<li><a href="MAPKAPK5" title="MAPKAPK5">MAPKAPK5</a></li>

<li><a href="OBSCN" class="mw-redirect" title="OBSCN">OBSCN</a></li>

<li><a href="Kalirin" title="Kalirin">Kalirin</a></li>

<li><a href="Titin" title="Titin">Titin</a></li>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Myosin_light-chain_kinase" title="Myosin light-chain kinase">Myosin light-chain kinase</a> (EC 2.7.11.18)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Phosphorylase_kinase" title="Phosphorylase kinase">Phosphorylase kinase</a> (EC 2.7.11.19)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Elongation_factor_2_kinase" title="Elongation factor 2 kinase">Elongation factor 2 kinase</a> (EC 2.7.11.20)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Polo_kinase" title="Polo kinase">Polo kinase</a> (EC 2.7.11.21)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks mw-collapsible mw-collapsed navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Serine/threonine-specific_protein_kinases_(EC_2.7.11.21-EC_2.7.11.30)102" style="font-size:114%;margin:0 4em"><a href="Serine/threonine-specific_protein_kinase" title="Serine/threonine-specific protein kinase">Serine/threonine-specific protein kinases</a> (EC 2.7.11.21-EC 2.7.11.30)</div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Polo_kinase" title="Polo kinase">Polo kinase</a> (EC 2.7.11.21)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Cyclin-dependent_kinase" title="Cyclin-dependent kinase">Cyclin-dependent kinase</a> (EC 2.7.11.22)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="(RNA-polymerase)-subunit_kinase" title="(RNA-polymerase)-subunit kinase">(RNA-polymerase)-subunit kinase</a> (EC 2.7.11.23)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<li><a href="P70S6_kinase" class="mw-redirect" title="P70S6 kinase">P70S6 kinase</a></li>

<li><a href="P70-S6_Kinase_1" title="P70-S6 Kinase 1">P70-S6 Kinase 1</a></li>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Mitogen-activated_protein_kinase" title="Mitogen-activated protein kinase">Mitogen-activated protein kinase</a> (EC 2.7.11.24)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Extracellular_signal-regulated_kinases" title="Extracellular signal-regulated kinases">Extracellular signal-regulated</a>

<li><a href="C-Jun_N-terminal_kinases" title="C-Jun N-terminal kinases">C-Jun N-terminal</a>

<li><a href="P38_mitogen-activated_protein_kinases" title="P38 mitogen-activated protein kinases">P38 mitogen-activated protein</a>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="MAP_kinase_kinase_kinase" title="MAP kinase kinase kinase">MAP3K</a> (EC 2.7.11.25)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="MAP_kinase_kinase_kinase" title="MAP kinase kinase kinase">MAP kinase kinase kinases</a>

<li>

<li>MLKs

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Tau-protein_kinase" title="Tau-protein kinase">Tau-protein kinase</a> (EC 2.7.11.26)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="(acetyl-CoA_carboxylase)_kinase" title="(acetyl-CoA carboxylase) kinase">(acetyl-CoA carboxylase) kinase</a> (EC 2.7.11.27)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Tropomyosin_kinase" title="Tropomyosin kinase">Tropomyosin kinase</a> (EC 2.7.11.28)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Low-density-lipoprotein_receptor_kinase" title="Low-density-lipoprotein receptor kinase">Low-density-lipoprotein receptor kinase</a> (EC 2.7.11.29)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Receptor_protein_serine/threonine_kinase" title="Receptor protein serine/threonine kinase">Receptor protein serine/threonine kinase</a> (EC 2.7.11.30)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Bone_morphogenetic_protein_receptors" class="mw-redirect" title="Bone morphogenetic protein receptors">Bone morphogenetic protein receptors</a>

<li><a href="ACVRL1" title="ACVRL1">ACVRL1</a></li>

<li><a href="Anti-M%C3%BCllerian_hormone_receptor" class="mw-redirect" title="Anti-Müllerian hormone receptor">Anti-Müllerian hormone receptor</a></li></ul>

</div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks mw-collapsible mw-collapsed navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Dual-specificity_kinases_(EC_2.7.12)102" style="font-size:114%;margin:0 4em"><a href="Dual-specificity_kinase" title="Dual-specificity kinase">Dual-specificity kinases</a> (EC 2.7.12)</div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="MAP2K49" scope="row" class="navbox-group" style="width:1%"><a href="Mitogen-activated_protein_kinase_kinase" title="Mitogen-activated protein kinase kinase">MAP2K</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr></tbody></table></div>

<div class="navbox-styles"></div><div role="navigation" class="navbox" aria-labelledby="Enzymes56" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Enzymes56" style="font-size:114%;margin:0 4em"><a href="Enzyme" title="Enzyme">Enzymes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Activity</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Active_site" title="Active site">Active site</a></li>

<li><a href="Binding_site" title="Binding site">Binding site</a></li>

<li><a href="Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li>

<li><a href="Oxyanion_hole" title="Oxyanion hole">Oxyanion hole</a></li>

<li><a href="Enzyme_promiscuity" title="Enzyme promiscuity">Enzyme promiscuity</a></li>

<li><a href="Diffusion-limited_enzyme" title="Diffusion-limited enzyme">Diffusion-limited enzyme</a></li>

<li><a href="Cofactor_(biochemistry)" title="Cofactor (biochemistry)">Cofactor</a></li>

<li><a href="Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Regulation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Allosteric_regulation" title="Allosteric regulation">Allosteric regulation</a></li>

<li><a href="Cooperativity" title="Cooperativity">Cooperativity</a></li>

<li><a href="Enzyme_inhibitor" title="Enzyme inhibitor">Enzyme inhibitor</a></li>

<li><a href="Enzyme_activator" title="Enzyme activator">Enzyme activator</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Classification</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Enzyme_Commission_number" title="Enzyme Commission number">EC number</a></li>

<li><a href="Protein_superfamily" title="Protein superfamily">Enzyme superfamily</a></li>

<li><a href="Protein_family" title="Protein family">Enzyme family</a></li>

<li><a href="List_of_enzymes" title="List of enzymes">List of enzymes</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Kinetics</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li>

<li><a href="Eadie%E2%80%93Hofstee_diagram" title="Eadie–Hofstee diagram">Eadie–Hofstee diagram</a></li>

<li><a href="Hanes%E2%80%93Woolf_plot" title="Hanes–Woolf plot">Hanes–Woolf plot</a></li>

<li><a href="Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk plot</a></li>

<li><a href="Michaelis%E2%80%93Menten_kinetics" title="Michaelis–Menten kinetics">Michaelis–Menten kinetics</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><b>EC1 <a href="Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a></b> (<a href="List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li>

<li><b>EC2 <a href="Transferase" title="Transferase">Transferases</a></b> (<a href="List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li>

<li><b>EC3 <a href="Hydrolase" title="Hydrolase">Hydrolases</a></b> (<a href="List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li>

<li><b>EC4 <a href="Lyase" title="Lyase">Lyases</a></b> (<a href="List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li>

<li><b>EC5 <a href="Isomerase" title="Isomerase">Isomerases</a></b> (<a href="List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li>

<li><b>EC6 <a href="Ligase" title="Ligase">Ligases</a></b> (<a href="List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li>

<li><b>EC7 <a href="Translocase" title="Translocase">Translocases</a></b> (<a href="List_of_EC_numbers_(EC_7)" title="List of EC numbers (EC 7)">list</a>)</li></ul>

</div></td></tr></tbody></table></div>

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